Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family
Autore:
Steinle, A; Li, PW; Morris, DL; Groh, V; Lanier, LL; Strong, RK; Spies, T;
Indirizzi:
Fred Hutchinson Canc Res Ctr, Div Clin Res, Seattle, WA 98109 USA Fred Hutchinson Canc Res Ctr Seattle WA USA 98109 , Seattle, WA 98109 USA Fred Hutchinson Canc Res Ctr, Div Basic Sci, Seattle, WA 98109 USA Fred Hutchinson Canc Res Ctr Seattle WA USA 98109 , Seattle, WA 98109 USA Univ Calif San Francisco, Dept Microbiol & Immunol, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 ancisco, CA 94143 USA Univ Calif San Francisco, Canc Res Inst, San Francisco, CA 94143 USA Univ Calif San Francisco San Francisco CA USA 94143 ancisco, CA 94143 USA
Titolo Testata:
IMMUNOGENETICS
fascicolo: 4, volume: 53, anno: 2001,
pagine: 279 - 287
SICI:
0093-7711(200105/06)53:4<279:IOHNWI>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRIPLET REPEAT POLYMORPHISM; CELL-SURFACE PROTEINS; CLASS-I MOLECULES; DELTA T-CELLS; NK CELLS; INHIBITORY RECEPTORS; ALLELIC REPERTOIRE; CRYSTAL-STRUCTURE; HLA-E; EXPRESSION;
Keywords:
NKG2D; ligand; N2DL; MIC; polymorphism;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Spies, T Fred Hutchinson Canc Res Ctr, Div Clin Res, 1100 Fairview Ave N, Seattle, WA 98109 USA Fred Hutchinson Canc Res Ctr 1100 Fairview Ave N Seattle WA USA 98109
Citazione:
A. Steinle et al., "Interactions of human NKG2D with its ligands MICA, MICB, and homologs of the mouse RAE-1 protein family", IMMUNOGENET, 53(4), 2001, pp. 279-287

Abstract

NKG213 is an activating receptor that is expressed on most natural killer (NK) cells, CD8 alpha beta T cells, and gamma delta T cells. Among its ligands is the distant major histocompatibility complex class I homolog MICA, which has no function in antigen presentation but is induced by cellular stress. To extend previous functional evidence, the NKG2D-MICA interaction wasstudied in isolation. NKG2D homodimers formed stable complexes with monomeric MICA in solution, demonstrating that no other components were required to facilitate this interaction. MICA glycosylation was not essential but enhanced complex formation. Soluble NKG213 also bound to cell surface MICB, which has structural and functional properties similar to those of MICA. Moreover, NKG2D stably interacted with surface molecules encoded by three newly identified cDNA sequences (N2DL-1 -2, and -3), which are identical to thehuman ULBP proteins and may represent homologs of the mouse retinoic acid-early inducible family of NKG213 ligands. Because of the substantial sequence divergence among these molecules, these results indicated promiscuous modes of receptor binding. Comparison of allelic variants of MICA revealed large differences in NKG2D binding that were associated with a single amino acid substitution at position 129 in the alpha2 domain. Varying affinities of MICA alleles for NKG213 may affect thresholds of NK-cell triggering and T-cell modulation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 08/07/20 alle ore 06:51:21